ARCA_BORBZ
ID ARCA_BORBZ Reviewed; 410 AA.
AC B7J0T5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Arginine deiminase {ECO:0000255|HAMAP-Rule:MF_00242};
DE Short=ADI {ECO:0000255|HAMAP-Rule:MF_00242};
DE EC=3.5.3.6 {ECO:0000255|HAMAP-Rule:MF_00242};
DE AltName: Full=Arginine dihydrolase {ECO:0000255|HAMAP-Rule:MF_00242};
DE Short=AD {ECO:0000255|HAMAP-Rule:MF_00242};
GN Name=arcA {ECO:0000255|HAMAP-Rule:MF_00242}; OrderedLocusNames=BbuZS7_0871;
OS Borreliella burgdorferi (strain ZS7) (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=445985;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZS7;
RX PubMed=20935092; DOI=10.1128/jb.01158-10;
RA Schutzer S.E., Fraser-Liggett C.M., Casjens S.R., Qiu W.G., Dunn J.J.,
RA Mongodin E.F., Luft B.J.;
RT "Whole-genome sequences of thirteen isolates of Borrelia burgdorferi.";
RL J. Bacteriol. 193:1018-1020(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-arginine = L-citrulline + NH4(+);
CC Xref=Rhea:RHEA:19597, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:32682, ChEBI:CHEBI:57743; EC=3.5.3.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00242};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC pathway; carbamoyl phosphate from L-arginine: step 1/2.
CC {ECO:0000255|HAMAP-Rule:MF_00242}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00242}.
CC -!- SIMILARITY: Belongs to the arginine deiminase family.
CC {ECO:0000255|HAMAP-Rule:MF_00242}.
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DR EMBL; CP001205; ACK74935.1; -; Genomic_DNA.
DR RefSeq; WP_002557431.1; NC_011728.1.
DR AlphaFoldDB; B7J0T5; -.
DR SMR; B7J0T5; -.
DR EnsemblBacteria; ACK74935; ACK74935; BbuZS7_0871.
DR GeneID; 56567419; -.
DR KEGG; bbz:BbuZS7_0871; -.
DR HOGENOM; CLU_052662_0_1_12; -.
DR OMA; ERATMHL; -.
DR OrthoDB; 592329at2; -.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000006901; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016990; F:arginine deiminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR GO; GO:0018101; P:protein citrullination; IEA:GOC.
DR HAMAP; MF_00242; Arg_deiminase; 1.
DR InterPro; IPR003876; Arg_deiminase.
DR PIRSF; PIRSF006356; Arg_deiminase; 1.
DR PRINTS; PR01466; ARGDEIMINASE.
DR TIGRFAMs; TIGR01078; arcA; 1.
PE 3: Inferred from homology;
KW Arginine metabolism; Cytoplasm; Hydrolase.
FT CHAIN 1..410
FT /note="Arginine deiminase"
FT /id="PRO_1000119036"
FT ACT_SITE 400
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ SEQUENCE 410 AA; 46844 MW; C2DF4F58E5848FAB CRC64;
MEEEYLNPIN IFSEIGRLKK VLLHRPGEEL ENLTPLIMKN FLFDDIPYLK VARQEHEVFV
NILKDNSVEI EYVEDLVSEV LASSVALKNK FISQFILEAE IKTDGVINIL KDYFSNLTVD
NMVSKMISGV AREELKDCEF SLDDWVNGSS LFVIDPMPNV LFTRDPFASI GNGITINKMY
TKVRRRETIF AEYIFKYHSA YKENVPIWFN RWEETSLEGG DEFVLNKDLL VIGISERTEA
GSVEKLAASL FKNKAPFSTI LAFKIPKNRA YMHLDTVFTQ IDYSVFTSFT SDDMYFSIYV
LTYNSNSNKI NIKKEKAKLK DVLSFYLGRK IDIIKCAGGD LIHGAREQWN DGANVLAIAP
GEVIAYSRNH VTNKLFEENG IKVHRIPSSE LSRGRGGPRC MSMSLVREDI